ID CRTAP_MOUSE Reviewed; 400 AA. AC Q9CYD3; O88698; Q8C8C5; DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 3. DT 24-JAN-2024, entry version 153. DE RecName: Full=Cartilage-associated protein; DE Flags: Precursor; GN Name=Crtap; Synonyms=Casp; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Embryo; RX PubMed=10429950; DOI=10.1016/s0945-053x(99)00002-5; RA Morello R., Tonachini L., Monticone M., Viggiano L., Rocchi M., RA Cancedda R., Castagnola P.; RT "cDNA cloning, characterization and chromosome mapping of Crtap encoding RT the mouse cartilage associated protein."; RL Matrix Biol. 18:319-324(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Embryo; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Olfactory epithelium; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP FUNCTION, TISSUE SPECIFICITY, AND INVOLVEMENT IN OSTEOCHONDRODYSPLASIA. RX PubMed=17055431; DOI=10.1016/j.cell.2006.08.039; RA Morello R., Bertin T.K., Chen Y., Hicks J., Tonachini L., Monticone M., RA Castagnola P., Rauch F., Glorieux F.H., Vranka J., Baechinger H.P., RA Pace J.M., Schwarze U., Byers P.H., Weis M., Fernandes R.J., Eyre D.R., RA Yao Z., Boyce B.F., Lee B.; RT "CRTAP is required for prolyl 3-hydroxylation and mutations cause recessive RT osteogenesis imperfecta."; RL Cell 127:291-304(2006). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Kidney, and Lung; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: Necessary for efficient 3-hydroxylation of fibrillar collagen CC prolyl residues. {ECO:0000269|PubMed:17055431}. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix. CC -!- TISSUE SPECIFICITY: Found in articular chondrocytes. Expressed in a CC variety of tissues. {ECO:0000269|PubMed:17055431}. CC -!- DISEASE: Note=Defects in Crtap are a cause of osteochondrodysplasia CC characterized by severe osteoporosis and decreased osteoid production. CC {ECO:0000269|PubMed:17055431}. CC -!- SIMILARITY: Belongs to the leprecan family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ006469; CAA07053.1; -; mRNA. DR EMBL; AK017797; BAB30938.1; -; mRNA. DR EMBL; AK047506; BAC33076.1; -; mRNA. DR EMBL; BC049890; AAH49890.1; -; mRNA. DR CCDS; CCDS23592.1; -. DR RefSeq; NP_064306.2; NM_019922.2. DR AlphaFoldDB; Q9CYD3; -. DR STRING; 10090.ENSMUSP00000081941; -. DR GlyConnect; 2188; 1 N-Linked glycan (1 site). DR GlyCosmos; Q9CYD3; 2 sites, 1 glycan. DR GlyGen; Q9CYD3; 2 sites, 1 N-linked glycan (1 site). DR iPTMnet; Q9CYD3; -. DR PhosphoSitePlus; Q9CYD3; -. DR EPD; Q9CYD3; -. DR MaxQB; Q9CYD3; -. DR PaxDb; 10090-ENSMUSP00000081941; -. DR PeptideAtlas; Q9CYD3; -. DR ProteomicsDB; 285365; -. DR Pumba; Q9CYD3; -. DR Antibodypedia; 27879; 276 antibodies from 29 providers. DR DNASU; 56693; -. DR Ensembl; ENSMUST00000084881.5; ENSMUSP00000081941.5; ENSMUSG00000032431.7. DR GeneID; 56693; -. DR KEGG; mmu:56693; -. DR UCSC; uc009rxg.2; mouse. DR AGR; MGI:1891221; -. DR CTD; 10491; -. DR MGI; MGI:1891221; Crtap. DR VEuPathDB; HostDB:ENSMUSG00000032431; -. DR eggNOG; KOG4459; Eukaryota. DR GeneTree; ENSGT00940000153814; -. DR HOGENOM; CLU_029887_0_1_1; -. DR InParanoid; Q9CYD3; -. DR OMA; WPETVEY; -. DR OrthoDB; 5398065at2759; -. DR PhylomeDB; Q9CYD3; -. DR TreeFam; TF320837; -. DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes. DR BioGRID-ORCS; 56693; 2 hits in 77 CRISPR screens. DR ChiTaRS; Crtap; mouse. DR PRO; PR:Q9CYD3; -. DR Proteomes; UP000000589; Chromosome 9. DR RNAct; Q9CYD3; Protein. DR Bgee; ENSMUSG00000032431; Expressed in vault of skull and 256 other cell types or tissues. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI. DR GO; GO:0005615; C:extracellular space; ISO:MGI. DR GO; GO:0032991; C:protein-containing complex; ISS:CAFA. DR GO; GO:0061077; P:chaperone-mediated protein folding; ISS:CAFA. DR GO; GO:0030199; P:collagen fibril organization; IBA:GO_Central. DR GO; GO:1901874; P:negative regulation of post-translational protein modification; ISO:MGI. DR GO; GO:0050821; P:protein stabilization; ISO:MGI. DR GO; GO:0007283; P:spermatogenesis; IEP:BHF-UCL. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR PANTHER; PTHR13986:SF3; CARTILAGE-ASSOCIATED PROTEIN; 1. DR PANTHER; PTHR13986; PROTEIN LYSINE HYDROXYLATION COMPLEX COMPONENT; 1. DR Genevisible; Q9CYD3; MM. PE 1: Evidence at protein level; KW Extracellular matrix; Glycoprotein; Hydroxylation; Reference proteome; KW Secreted; Signal. FT SIGNAL 1..25 FT /evidence="ECO:0000255" FT CHAIN 26..400 FT /note="Cartilage-associated protein" FT /id="PRO_0000006320" FT CARBOHYD 86 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 362 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CONFLICT 7 FT /note="T -> A (in Ref. 1; CAA07053)" FT /evidence="ECO:0000305" FT CONFLICT 34 FT /note="S -> N (in Ref. 1; CAA07053)" FT /evidence="ECO:0000305" FT CONFLICT 79..80 FT /note="SE -> RQ (in Ref. 2; BAB30938)" FT /evidence="ECO:0000305" FT CONFLICT 249..250 FT /note="SR -> VA (in Ref. 2; BAB30938)" FT /evidence="ECO:0000305" FT CONFLICT 254 FT /note="D -> T (in Ref. 2; BAB30938)" FT /evidence="ECO:0000305" SQ SEQUENCE 400 AA; 46169 MW; F6080CEC275CC5A4 CRC64; MGPRSPTAAL LVLLCVGCAP TPGRGQYERY SFRSFPRDEL MPLESAYRHA LDQYSGEHWA ESVGYLEVSL RLHRLLRDSE AFCHRNCSAA TPAPAPAGPA SHAELRLFGS VLRRAQCLKR CKQGLPAFRQ SQPSRSVLAD FQQREPYKFL QFAYFKANDL PKAIAAAHTY LLKHPDDEMM KRNMEYYKSL PGAEDHIKDL ETKSYESLFV RAVRAYNGEN WRTSISDMEL ALPDFLKAFY ECLAACEGSR EIKDFKDFYL SIADHYVEVL ECKIRCEETL TPVIGGYPVE KFVATMYHYL QFAYYKLNDL KNAAPCAVSY LLFDQSDRVM QQNLVYYQYH RDKWGLSDEH FQPRPEAVQF FNVTTLQKEL YDFAQEHLMD DDEGEVVEYV DDLLETEESA //